PMID- 8092987
OWN - NLM
STAT- MEDLINE
DCOM- 19941014
LR  - 20190501
IS  - 0264-6021 (Print)
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 302 ( Pt 2)
IP  - Pt 2
DP  - 1994 Sep 1
TI  - Purification and characterization of the human epidermal fatty acid-binding 
      protein: localization during epidermal cell differentiation in vivo and in vitro.
PG  - 363-71
AB  - Epidermal fatty acid-binding protein (E-FABP) was isolated from human skin and 
      purified to homogeneity. Its molecular mass was estimated to be 15 kDa and the pI 
      of non-denaturing protein was 5.6. Scatchard-plot analysis revealed one class of 
      binding site for oleic acid with a Kd of 0.46 microM. Structure-binding relation 
      experiments revealed a high affinity of E-FABP for stearic acid which decreased 
      on reduction of the number of carbon atoms or introduction of double bonds into 
      the fatty acid chain. Squalene, cholesterol and retinoic acid isomers showed no 
      affinity, suggesting that E-FABP displays high specificity for fatty acids. 
      E-FABP is a scarce cytosolic protein (0.065% of total protein). Only trace 
      amounts could be detected in normal human skin but up to 42.5 +/- 3.4 pmol/mg of 
      protein was found in a non-malignant defect of keratinocyte differentiation 
      (psoriatic lesions). E-FABP levels were low in cultured human keratinocytes grown 
      under proliferation-stimulating conditions but increased about 2-fold on 
      induction of differentiation by Ca2+. Immunohistochemical localization showed 
      cytosolic staining in differentiated cells of normal and psoriatic skin, 
      suggesting a link between E-FABP and keratinocyte differentiation. The presence 
      of E-FABP in tissues other than skin (heart, intestine and adipose tissue) 
      excludes its specific role in fatty acid metabolism in epithelial cells or its 
      involvement in skin lipid-barrier function.
FAU - Siegenthaler, G
AU  - Siegenthaler G
AD  - Clinique de Dermatologie, Hopital Cantonal Universitaire, Geneve, Switzerland.
FAU - Hotz, R
AU  - Hotz R
FAU - Chatellard-Gruaz, D
AU  - Chatellard-Gruaz D
FAU - Didierjean, L
AU  - Didierjean L
FAU - Hellman, U
AU  - Hellman U
FAU - Saurat, J H
AU  - Saurat JH
LA  - eng
PT  - Journal Article
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Carrier Proteins)
RN  - 0 (FABP5 protein, human)
RN  - 0 (FABP7 protein, human)
RN  - 0 (Fatty Acid-Binding Protein 7)
RN  - 0 (Fatty Acid-Binding Proteins)
RN  - 0 (Fatty Acids)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Tumor Suppressor Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Carrier Proteins/*analysis/chemistry/isolation & purification
MH  - Cell Differentiation
MH  - Cells, Cultured
MH  - Chromatography, Affinity
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Epidermal Cells
MH  - Epidermis/*chemistry/pathology
MH  - Fatty Acid-Binding Protein 7
MH  - Fatty Acid-Binding Proteins
MH  - Fatty Acids/*metabolism
MH  - Humans
MH  - Immunoblotting
MH  - Immunohistochemistry
MH  - Isoelectric Focusing
MH  - Keratinocytes/*chemistry/cytology/pathology
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - *Neoplasm Proteins
MH  - Psoriasis/*metabolism/pathology
MH  - Tissue Distribution
MH  - *Tumor Suppressor Proteins
PMC - PMC1137237
EDAT- 1994/09/01 00:00
MHDA- 1994/09/01 00:01
PMCR- 1994/09/01
CRDT- 1994/09/01 00:00
PHST- 1994/09/01 00:00 [pubmed]
PHST- 1994/09/01 00:01 [medline]
PHST- 1994/09/01 00:00 [entrez]
PHST- 1994/09/01 00:00 [pmc-release]
AID - 10.1042/bj3020363 [doi]
PST - ppublish
SO  - Biochem J. 1994 Sep 1;302 ( Pt 2)(Pt 2):363-71. doi: 10.1042/bj3020363.